Docking Study of Chromone Derivatives as HIV-1 Protease Inhibitors Jiraporn Ungwitayatorn and Weerasak Samee
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A series of non-peptide HIV-1 protease (HIV-1 PR) inhibitors, chromone derivatives, were docked with the HIV-1 protease binding site for study the binding interaction. The orientation of chromone molecules showed the critical interaction which are important for the inhibition of the enzyme. The chromone molecules form hydrogen bonding interaction with Asp25, Asp25', Ile50 and Ile50' and hydrophobic interaction with Val32,Ile50,Pro81, Val82, and Ile84. The binding energies of 35 chromone derivatives were subjected to quantitative structure-activity relationship (QSAR) study using multiple linear regression (MLR) to correlate the inhibitory activity and the binding energies. A good linear correlation was found with the r2 value of 0.9405
Keyword:
Docking Study , Chromone, HIV-1 Protease ,HIV-1 PR,hydrophobic interaction
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